Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Balciunas D, Ronne H
- Evidence of domain swapping within the jumonji family of transcription factors.
- Trends Biochem Sci. 2000; 25: 274-6
- Dunwell JM, Khuri S, Gane PJ
- Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamily.
- Microbiol Mol Biol Rev. 2000; 64: 153-79
- Display abstract
This review summarizes the recent discovery of the cupin superfamily (from the Latin term "cupa," a small barrel) of functionally diverse proteins that initially were limited to several higher plant proteins such as seed storage proteins, germin (an oxalate oxidase), germin-like proteins, and auxin-binding protein. Knowledge of the three-dimensional structure of two vicilins, seed proteins with a characteristic beta-barrel core, led to the identification of a small number of conserved residues and thence to the discovery of several microbial proteins which share these key amino acids. In particular, there is a highly conserved pattern of two histidine-containing motifs with a varied intermotif spacing. This cupin signature is found as a central component of many microbial proteins including certain types of phosphomannose isomerase, polyketide synthase, epimerase, and dioxygenase. In addition, the signature has been identified within the N-terminal effector domain in a subgroup of bacterial AraC transcription factors. As well as these single-domain cupins, this survey has identified other classes of two-domain bicupins including bacterial gentisate 1, 2-dioxygenases and 1-hydroxy-2-naphthoate dioxygenases, fungal oxalate decarboxylases, and legume sucrose-binding proteins. Cupin evolution is discussed from the perspective of the structure-function relationships, using data from the genomes of several prokaryotes, especially Bacillus subtilis. Many of these functions involve aspects of sugar metabolism and cell wall synthesis and are concerned with responses to abiotic stress such as heat, desiccation, or starvation. Particular emphasis is also given to the oxalate-degrading enzymes from microbes, their biological significance, and their value in a range of medical and other applications.
- Ponting CP
- Evidence for PDZ domains in bacteria, yeast, and plants.
- Protein Sci. 1997; 6: 464-8
- Display abstract
Several dozen signaling proteins are now known to contain 80-100 residue repeats, called PDZ (or DHR or GLGF) domains, several of which interact with the C-terminal tetrapeptide motifs X-Ser/Thr-X-Val-
SMART accession number: SM01093 Description: - Interpro abstract (IPR003823): This entry represents an uncharacterised domain found in calvin cycle protein CP12 and other proteins. This domain is sometimes found in association cystathionine-beta-synthase domains. Family alignment:
Click on the following links for more information.
- Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing CP12 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with CP12 domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing CP12 domain in the selected taxonomic class.
- Structure (3D structures containing this domain)
3D Structures of CP12 domains in PDB
PDB code Main view Title 2lj9 Partial 3d structure of the c-terminal part of the free arabidopsis thaliana cp12-2 in its oxidized form 3qv1 Crystal structure of the binary complex of photosyntetic A4 glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with cp12-2, both from Arabidopsis thaliana. 3rvd Crystal structure of the binary complex, obtained by soaking, of photosyntetic a4 glyceraldehyde 3-phosphate dehydrogenase (gapdh) with cp12-2, both from arabidopsis thaliana.
- Links (links to other resources describing this domain)
PFAM CP12 INTERPRO IPR003823